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. 2017 Aug 31;30(9):685–696. doi: 10.1093/protein/gzx044

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© The Author 2017. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 8 — Analysis of pairing of light to heavy chain in the bsAb B10v5 × huOKT3 by LC–ESI–MS, after protein A purification and deglycosylation. The bsAbs contained either no mutation in the Fab interface (wildtype) or contained mutations in the C_H1:C_L interface (see Table I for a complete list). The V_H:V_L interface was left unmutated in all cases. The antibodies were produced by transient transfection of HEK293-6E. The prevalence of correctly assembled bsAb is given in percent of all detected heterodimeric IgGs and represents a mean of three independent transfections (Table IV).